6 - Fig. 5-25 Lehn Fig. 5-25 Lehn Fig. 5-25 Lehn Fig. 5-25...

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Fig. 4-29 Lehn
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Protein disulfide isomerase Peptide prolyl isomerase Chaperones
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• ‘Tail-to-tail’ heptamers • Cage for folding GroEL/GroES (Hsp60/Hsp10)
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Fig. 4-31 Lehn
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Amyloidoses Diseases where mutant forms of normally occurring proteins accumulate in tissues as AMYLOID (insoluble aggregates) 2 very different stable protein conformations Native form Amyloid form
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β -cross Fibers: helical arrangement of β -strands perpendicular to the fiber axis Protein fibrils rich in β - sheets, even though native state of the proteins may lack β -sheets Large number of fibrils adopt β -cross conformation
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Taylor et al. Science 296:1991(0
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Protein Structure and Function in the Immune System
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Fig. 15-1 B and T
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Fig. 5-21 Lehn
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V L C L V H C H 1 Fig. 15-6 B and T
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Fig. 5-21 Lehn
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Fig. 5-21 Lehn
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Unformatted text preview: Fig. 5-25 Lehn Fig. 5-25 Lehn Fig. 5-25 Lehn Fig. 5-25 Lehn Fig. 15-18 B and T MHC Proteins Highly polymorphic set of proteins in population Help discriminate between self and non-self Involved in both cell mediated and humoral immune response Bind peptide fragments of proteins and present them to T cells Found on virtually all of our cells Help define uniqueness of individual Fig. 15-18 B and T MHC Class I structure Membrane Protein 2 Polypeptide Chains Heavy Chain: 3 domains 1, 2, 3 Light Chain: 1 domain 2 microglobulin 3 and 2 microglobulin domains show structural similarity to Ig Constant domains BUT 1 and 2 domains are completely different Fig. 5-21 Lehn Fig. 5-21 Lehn Fig. 15-19 B and T Fig. 5-22 Lehn 4th Fig. 15-20 B and T Fig. 15-18 B and T...
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6 - Fig. 5-25 Lehn Fig. 5-25 Lehn Fig. 5-25 Lehn Fig. 5-25...

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